TABLE 1.

Crystallographic data collection and refinement statistics

	Structure 1	Structure 2	Structure 3	Structure 4
Data collection
Space group	C2	C2	P212121	C2
Cell dimensions
a, b, c	141.6, 102.8, 59.2 Å	141.6, 102.6, 60.0 Å	84.5, 87.4, 185.5 Å	141.6, 102.9, 59.1 Å
α, β, γ	112.4	112.8		112.6
Resolution	40.0/1.9 (2.0/1.9 Å)a	40.0/2.3 Å (2.4/2.3 Å)a	30.0/3.1 Å (3.2/3.1 Å)a	40.0/1.9 Å (2.0/1.9 Å)a
Rmerge	0.07 (0.32)a	0.1 (0.4)a	0.1 (0.5)a	0.1 (0.4)a
I/σI	12.2 (3.2)a	18.4 (3.8)a	11.8 (2.6)a	9.6 (5.4)a
Completeness	90.1% (92.6%)a	100% (99.9%)a	99.3% (99.2%)a	100% (99.7%)a
Redundancy	3.0 (2.8)a	8.1 (7.8)a	7.1 (7.0)a	5.7 (5.7)a
Refinement
Resolution	40.0/1.9 Å	40.0/2.3 Å	30.0/3.1 Å	40.0/1.9 Å
No. of reflections	52,728	33,294	24,221	58,385
Rwork/Rfree	0.19/0.21	0.19/0.23	0.22/0.29	0.18/0.19
No. of atoms	4863	4936	9174	5008
Protein	4502	4502	9031	4504
Ligand/ion	106	249	143	139
Water	255	185	0	365
B-Wilson	19.0	35.1	63.4	14.6
B factors
Overall	18.6 Å2	22.5 Å2	43.5 Å2	14.6 Å2
Main chain	17.6 Å2	20.1 Å2	43.3 Å2	13.0 Å2
Side chains	19.6 Å2	24.7 Å2	43.7 Å2	16.1 Å2
Root mean square deviations
Bond lengths	0.008 Å	0.011 Å	0.009 Å	0.007 Å
Bond angles	1.064°	1.302°	1.164°	0.978°
Model quality
Ramachandran plot
Most favored	91.4%	91.0%	86.3%	92.6%
Additional allowed	8.4%	9.0%	13.5%	7.2%
Generously allowed	0.2%	0%	0.3%	0.2%

^a Values in parentheses refer to the highest resolution shell.